1994
DOI: 10.1038/372739a0
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A protein kinase involved in the regulation of inflammatory cytokine biosynthesis

Abstract: Production of interleukin-1 and tumour necrosis factor from stimulated human monocytes is inhibited by a new series of pyridinyl-imidazole compounds. Using radiolabelled and radio-photoaffinity-labelled chemical probes, the target of these compounds was identified as a pair of closely related mitogen-activated protein kinase homologues, termed CSBPs. Binding of the pyridinyl-imidazole compounds inhibited CSBP kinase activity and could be directly correlated with their ability to inhibit cytokine production, su… Show more

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Cited by 3,172 publications
(2,440 citation statements)
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References 41 publications
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“…Various other studies implying p38 MAP kinase in AP-1 regulation (Hazzalin et al, 1996(Hazzalin et al, , 1997 suggest that p38 MAP kinase may also be involved in okadaic acid induced AP-1 activation. To test this hypothesis we used SB 203580, a pyridinyl-imidazole compound described as speci®c inhibitor of this enzyme (Lee et al, 1994;Cuenda et al, 1995), in an attempt to block p38 MAP kinase activation. To assure that under the experimental conditions used, SB 203580 inhibited p38 MAPK and to con®rm its speci®city we treated exponentially growing 308 cells with this inhibitor (or the solvent dimethyl sulfoxide, DMSO) for 1 h prior to the addition of 100 ng/ml okadaic acid (or DMSO).…”
Section: Resultsmentioning
confidence: 99%
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“…Various other studies implying p38 MAP kinase in AP-1 regulation (Hazzalin et al, 1996(Hazzalin et al, , 1997 suggest that p38 MAP kinase may also be involved in okadaic acid induced AP-1 activation. To test this hypothesis we used SB 203580, a pyridinyl-imidazole compound described as speci®c inhibitor of this enzyme (Lee et al, 1994;Cuenda et al, 1995), in an attempt to block p38 MAP kinase activation. To assure that under the experimental conditions used, SB 203580 inhibited p38 MAPK and to con®rm its speci®city we treated exponentially growing 308 cells with this inhibitor (or the solvent dimethyl sulfoxide, DMSO) for 1 h prior to the addition of 100 ng/ml okadaic acid (or DMSO).…”
Section: Resultsmentioning
confidence: 99%
“…They bind in the ATP pocket of p38 MAP kinases and block their intrinsic ATPase activity (Lee et al, 1994;Cuenda et al, 1995). Binding to ERK-1/2 and JNKs could not be detected and even at high concentrations activities of these kinases have not been found to be a ected.…”
Section: Discussionmentioning
confidence: 99%
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“…We further examined the e ect of the p38 inhibitor on UVB induced p38 activation. The p38 inhibitor SB202190 does not a ect phosphorylation of p38 (data not shown) since the inhibitor only binds to the ATP pocket of p38 and blocks its intrinsic ATPase activity without a ecting its phosphorylation sites (Lee et al, 1994;Cuenda et al, 1995). In addition, the inhibition of p38 by SB202190 was reversible, therefore, the inhibitory e ect could not be detected by in vitro kinase assay of p38 (data not shown, Young et al, 1997;Wilson et al, 1997).…”
Section: Uvb Signi®cantly Activated P38 and Erkmentioning
confidence: 90%
“…JNKs are activated by two distinct MAPKKs, MKK4/SEK1 (Sanchez et al, 1994;Derijard et al, 1995), and MKK7 Yao et al, 1997;Wu et al, 1997;Tournier et al, 1997;Holland et al, 1997), in the JNK signaling unit. The p38 subgroup is composed of four genes including p38a, p38b, p38g and p38d (Han et al, 1994;Lee et al, 1994;Jiang et al, 1997;Stein et al, 1997;Goedert et al, 1997;Wang et al 1997). The p38s are also activated by at least two MAPKKs, MKK3 and MKK6 (Stein et al, 1996;Moriguchi et al, 1996).…”
Section: Upstream Kinases In the Jnk And P38 Modulesmentioning
confidence: 99%